If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Degradation/Utilization/Assimilation → Nucleosides and Nucleotides Degradation|
E. coli can use all three naturally occurring purine deoxyribonucleosides (deoadenosine, deoxyguanosine, and deoxyinosine) as total sources of carbon and energy. All are cleaved by the same deoD-encoded phosphorylase, yielding the corresponding bases (adenine, guanine and hypoxanthine) and D-deoxyribose-1-phosphate, which is converted to D-deoxyribose-5-phosphate by a mutase that also can utilize D-ribose-1-phosphate as a substrate. A specific aldolase splits D-deoxyribose-5-phosphate, yielding D-glyceraldehyde-3-phosphate, which enters central metabolism through the glycolytic pathway, and acetaldehyde, which must be converted to acetyl-CoA before it can enter central metabolism.
Although E. coli is able to utilize the deoxyribose moiety of deoxyribonucleosides, it is unable to utilize exogenously supplied deoxyribose; however, the closely related organism Salmonella typhimurium can.
The amino nitrogen of adenine and guanine but not the nitrogen atoms in the purine bases can serve as total sources of nitrogen for E. coli.
Review: Linn, E.C.C. Dissimilatory Pathways for Sugars, Polyols, and Carboxylates. E. coli and Salmonella, F.C. Neidhardt, Ed. [Neidhardt96]
Neidhardt96: Neidhardt FC, Curtiss III R, Ingraham JL, Lin ECC, Low Jr KB, Magasanik B, Reznikoff WS, Riley M, Schaechter M, Umbarger HE "Escherichia coli and Salmonella, Cellular and Molecular Biology, Second Edition." American Society for Microbiology, Washington, D.C., 1996.
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Ahmad69: Ahmad SI, Pritchard RH (1969). "A map of four genes specifying enzymes involved in catabolism of nucleosides and deoxynucleosides in Escherichia coli." Mol Gen Genet 104(4);351-9. PMID: 4904508
Aristarkhov96: Aristarkhov A, Mikulskis A, Belasco JG, Lin EC (1996). "Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli." J Bacteriol 178(14);4327-32. PMID: 8763968
Bennett03: Bennett EM, Li C, Allan PW, Parker WB, Ealick SE (2003). "Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase." J Biol Chem 278(47);47110-8. PMID: 12937174
Bennett03a: Bennett EM, Anand R, Allan PW, Hassan AE, Hong JS, Levasseur DN, McPherson DT, Parker WB, Secrist JA, Sorscher EJ, Townes TM, Waud WR, Ealick SE (2003). "Designer gene therapy using an Escherichia coli purine nucleoside phosphorylase/prodrug system." Chem Biol 10(12);1173-81. PMID: 14700625
Bertosa14: Bertoša B, Mikleušević G, Wielgus-Kutrowska B, Narczyk M, Hajnic M, Leščić Ašler I, Tomic S, Luic M, Bzowska A (2014). "Homooligomerization is needed for stability: a molecular modelling and solution study of Escherichia coli purine nucleoside phosphorylase." FEBS J 281(7);1860-71. PMID: 24785777
Bezirdzhian86: Bezirdzhian KhO, Kocharian ShM, Akopian ZhI (1986). "[Isolation of the hexameric form of purine nucleoside phosphorylase from E. coli. Comparative study of trimeric and hexameric forms of the enzyme]." Biokhimiia 1986;51(7);1085-92. PMID: 3089333
Bezirdzhian87: Bezirdzhian KhO, Kocharian ShM, Akopian ZhI (1987). "[Hexameric purine nucleoside phosphorylase II from Escherichia coli K-12. Physico-chemical and catalytic properties and stabilization with substrates]." Biokhimiia 1987;52(10);1624-31. PMID: 3122852
Buxton75: Buxton RS (1975). "Genetic analysis of thymidine-resistant and low-thymine-requiring mutants of Escherichia coli K-12 induced by bacteriophage Mu-1." J Bacteriol 121(2);475-84. PMID: 1089630
Chang91: Chang ZY, Nygaard P, Chinault AC, Kellems RE (1991). "Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function." Biochemistry 30(8);2273-80. PMID: 1998686
Dandanell05: Dandanell G, Szczepanowski RH, Kierdaszuk B, Shugar D, Bochtler M (2005). "Escherichia coli purine nucleoside phosphorylase II, the product of the xapA gene." J Mol Biol 348(1);113-25. PMID: 15808857
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